3VWU

Crystal structure of peroxiredoxin 4 from M. musculus

Summary for 3VWU

• Entry DOI: 10.2210/pdb3vwu/pdb
• Related: 3TJB 3TJF 3TJG 3VWV 3VWW 3W8J
• Descriptor: Peroxiredoxin-4 (1 entity in total)
• Functional Keywords: peroxiredoxin family, thioredoxin fold, peroxiredoxin, oxidoreductase
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm (By similarity): O08807
• Total number of polymer chains: 10
• Total formula weight: 287804.86

Authors

Inaba, K.,Suzuki, M. (deposition date: 2012-09-03, release date: 2013-09-04, Last modification date: 2024-11-13)

Primary citation

Sato, Y.,Kojima, R.,Okumura, M.,Hagiwara, M.,Masui, S.,Maegawa, K.,Saiki, M.,Horibe, T.,Suzuki, M.,Inaba, K.
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
Sci Rep, 3:2456-2456, 2013

PubMed Abstract: The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1α and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding. Here, we clarified the Prx4 preferential recognition of two PDI family proteins, P5 and ERp46, and the mode of interaction between Prx4 and P5 thioredoxin domain. Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides. Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding. Thus, the mammalian ER seems to contain highly systematized oxidative networks for the efficient production of large quantities of secretory proteins.

PubMed: 23949117
DOI: 10.1038/srep02456

Experimental method

X-RAY DIFFRACTION (3.3 Å)